期刊
FEBS LETTERS
卷 580, 期 22, 页码 5301-5305出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2006.08.075
关键词
caveolin scaffolding domain; membrane interface; NMR
Circular dichroism (CD) and NMR spectroscopy were used to study the conformational properties of two synthetic peptides, D82-R101 and D82-I109, encompassing the caveolin scaffolding domain (D82-R101), in the presence of dodecylphosphocholine (DPC) micelles. Our data show that a stable helical conformation of the caveolin scaffolding domain in a membrane mimicking system is only obtained for the peptide including the L102-I109 hydrophobic stretch, a part of the caveolin intra-membrane domain. Through chemical shift variations, an ensemble of six residues of the D82-L109 peptide, mainly located in the V94TKYWFYR101, motif were found to detect the presence of phosphatidylserine solubilized in DPC micelles. Our results constitute a first step for elucidating at a residue level the conformational properties of the central region of the caveolin-1 protein. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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